Overview

Description

  • NatureRecombinant
  • SourceE. coli
  • Amino Acid Sequence
    • SpeciesHuman
    • SequenceLTNSEPLDLDFSIQVLSSGSWPFQQSCTFALPSELERSYQRFTAFYASRH SG RKLTWLYQLSKGELVTNCFKNRYTLQASTFQMAILLQYNTEDAYTV QQLTDS TQIKMDILAQVLQILLKSKLLVLEDENANVDEVELKPDTLIK LYLGYKNKKL RVNINVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRI MKMRKVLKHQQLLG EVLTQLSSRFKPRVPVIKKCIDILIEKEYLERVD GEKDTYSYLA
    • Amino acids525 to 776

Specifications

Our Abpromise guarantee covers the use of ab91876 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

    Mass Spectrometry

  • FormLyophilised
  • Additional NotesProtein Identity confirmed by Mass Spectrometry (MS/MS) (acquired on initial reference batch).
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 0.5% Trehalose, 6M Urea, 100mM Sodium phosphate, 10mM Sodium chloride, pH 4.5

  • ReconstitutionReconstitute with 83 µl aqua dest.

General info

  • Alternative names
    • CUL 1
    • CUL-1
    • CUL1
    • CUL1_HUMAN
    • Cullin-1
    • Cullin1
    • MGC149834
    • MGC149835
    see all
  • FunctionCore component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(Cyclin F) directs ubiquitination of CP110.
  • Tissue specificityExpressed in lung fibroblasts.
  • PathwayProtein modification; protein ubiquitination.
  • Sequence similaritiesBelongs to the cullin family.
  • Post-translational
    modifications
    Neddylated; which enhances the ubiquitination activity of SCF. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. Deneddylated by Epstein-Barr virus BPLF1 leading to a S-phase-like environment that is required for efficient replication of the viral genome.
  • Information by UniProt

Human Cullin 1 protein fragment images

  • The image shows an electrophoretic assay performed using an Agilent 5100 ALP. In some images coloured control bands can be seen at 15 kDa (green) and/or 240 kDa (purple). The protein-specific band is blue.

References for Human Cullin 1 protein fragment (ab91876)

ab91876 has not yet been referenced specifically in any publications.

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